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P21243

- PSA1_YEAST

UniProt

P21243 - PSA1_YEAST

Protein

Proteasome subunit alpha type-1

Gene

SCL1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 168 (01 Oct 2014)
      Sequence version 1 (01 May 1991)
      Previous versions | rss
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    Functioni

    The proteasome degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. It has an ATP-dependent proteolytic activity.

    Catalytic activityi

    Cleavage of peptide bonds with very broad specificity.PROSITE-ProRule annotation

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. threonine-type endopeptidase activity Source: UniProtKB-KW

    GO - Biological processi

    1. proteasomal ubiquitin-independent protein catabolic process Source: SGD
    2. proteasome-mediated ubiquitin-dependent protein catabolic process Source: SGD

    Keywords - Molecular functioni

    Hydrolase, Protease, Threonine protease

    Enzyme and pathway databases

    BioCyciYEAST:G3O-30533-MONOMER.
    ReactomeiREACT_100522. Regulation of activated PAK-2p34 by proteasome mediated degradation.
    REACT_189025. ER-Phagosome pathway.
    REACT_189047. Cross-presentation of soluble exogenous antigens (endosomes).
    REACT_189060. Antigen processing: Ubiquitination & Proteasome degradation.
    REACT_189250. AUF1 (hnRNP D0) destabilizes mRNA.
    REACT_83036. Orc1 removal from chromatin.

    Protein family/group databases

    MEROPSiT01.971.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proteasome subunit alpha type-1 (EC:3.4.25.1)
    Alternative name(s):
    Macropain subunit C7-alpha
    Multicatalytic endopeptidase complex C7
    Proteasome component C7-alpha
    Proteasome component Y8
    Proteinase YSCE subunit 7
    SCL1 suppressor protein
    Gene namesi
    Name:SCL1
    Synonyms:PRC2, PRS2
    Ordered Locus Names:YGL011C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome VII

    Organism-specific databases

    CYGDiYGL011c.
    SGDiS000002979. SCL1.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: SGD
    2. nuclear outer membrane-endoplasmic reticulum membrane network Source: SGD
    3. nucleus Source: SGD
    4. proteasome core complex, alpha-subunit complex Source: SGD
    5. proteasome storage granule Source: SGD

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Proteasome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 252251Proteasome subunit alpha type-1PRO_0000124141Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei237 – 2371Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP21243.
    PaxDbiP21243.
    PeptideAtlasiP21243.
    PRIDEiP21243.

    2D gel databases

    UCD-2DPAGEP21243.

    Expressioni

    Gene expression databases

    GenevestigatoriP21243.

    Interactioni

    Subunit structurei

    The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. The catalytic chamber with the active sites is on the inside of the barrel. Interacts with CIC1.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PRE10P212426EBI-13975,EBI-13963
    PRE8P236396EBI-13975,EBI-13959

    Protein-protein interaction databases

    BioGridi33235. 74 interactions.
    DIPiDIP-2810N.
    IntActiP21243. 28 interactions.
    MINTiMINT-525412.

    Structurei

    Secondary structure

    1
    252
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi11 – 144
    Beta strandi16 – 183
    Turni21 – 233
    Helixi26 – 349
    Turni35 – 384
    Beta strandi42 – 465
    Beta strandi48 – 569
    Beta strandi62 – 643
    Helixi66 – 683
    Beta strandi71 – 744
    Beta strandi76 – 783
    Beta strandi80 – 856
    Helixi87 – 10822
    Helixi114 – 13017
    Beta strandi131 – 1344
    Beta strandi140 – 1478
    Turni148 – 1503
    Beta strandi151 – 1577
    Turni159 – 1613
    Beta strandi163 – 17210
    Helixi175 – 18915
    Beta strandi191 – 1933
    Helixi199 – 21416
    Beta strandi222 – 2298
    Beta strandi232 – 2354
    Helixi238 – 24811
    Turni249 – 2513

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FNTX-ray3.20A/O1-252[»]
    1G0UX-ray2.40G/U1-252[»]
    1G65X-ray2.25G/U10-252[»]
    1JD2X-ray3.002/G10-252[»]
    1RYPX-ray1.90A/O10-252[»]
    1VSYX-ray3.00A/O10-252[»]
    1Z7QX-ray3.22A/O1-252[»]
    2F16X-ray2.80G/U10-252[»]
    2FAKX-ray2.80G/U10-252[»]
    2GPLX-ray2.81G/U10-252[»]
    2ZCYX-ray2.90G/U1-252[»]
    3BDMX-ray2.70G/U1-252[»]
    3D29X-ray2.60G/U12-252[»]
    3DY3X-ray2.81G/U10-252[»]
    3DY4X-ray2.80G/U10-252[»]
    3E47X-ray3.00G/U10-252[»]
    3GPJX-ray2.70G/U10-252[»]
    3GPTX-ray2.41G/U10-252[»]
    3GPWX-ray2.50G/U10-252[»]
    3HYEX-ray2.50G/U10-252[»]
    3L5QX-ray3.00A/C10-252[»]
    3MG0X-ray2.68G/U10-252[»]
    3MG4X-ray3.11G/U10-252[»]
    3MG6X-ray2.60G/U1-252[»]
    3MG7X-ray2.78G/U1-252[»]
    3MG8X-ray2.59G/U1-252[»]
    3NZJX-ray2.40G/U1-252[»]
    3NZWX-ray2.50G/U1-252[»]
    3NZXX-ray2.70G/U1-252[»]
    3OEUX-ray2.60G/U10-252[»]
    3OEVX-ray2.85G/U10-252[»]
    3OKJX-ray2.70G/U10-252[»]
    3SDIX-ray2.65G/U10-252[»]
    3SDKX-ray2.70G/U10-252[»]
    3SHJX-ray2.80G/U10-252[»]
    3TDDX-ray2.70G/U10-252[»]
    3UN4X-ray3.40G/U1-252[»]
    3UN8X-ray2.70G/U1-252[»]
    4CR2electron microscopy7.70A1-252[»]
    4CR3electron microscopy9.30A1-252[»]
    4CR4electron microscopy8.80A1-252[»]
    4EU2X-ray2.51A/O10-250[»]
    4FZCX-ray2.80G/U10-252[»]
    4FZGX-ray3.00G/U10-252[»]
    4G4SX-ray2.49A1-252[»]
    4GK7X-ray2.80G/U10-252[»]
    4HNPX-ray2.80G/U10-252[»]
    4HRCX-ray2.80G/U10-252[»]
    4HRDX-ray2.80G/U10-252[»]
    4INRX-ray2.70G/U1-252[»]
    4INTX-ray2.90G/U1-252[»]
    4INUX-ray3.10G/U1-252[»]
    4J70X-ray2.80G/U1-252[»]
    4JSQX-ray2.80G/U1-252[»]
    4JSUX-ray2.90G/U1-252[»]
    4JT0X-ray3.10G/U1-252[»]
    4LQIX-ray2.70G/U10-252[»]
    4NNNX-ray2.50G/U1-252[»]
    4NNWX-ray2.60G/U1-252[»]
    4NO1X-ray2.50G/U1-252[»]
    4NO6X-ray3.00G/U1-252[»]
    4NO8X-ray2.70G/U1-252[»]
    4NO9X-ray2.90G/U1-252[»]
    4QBYX-ray3.00G/U1-252[»]
    ProteinModelPortaliP21243.
    SMRiP21243. Positions 10-252.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP21243.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1A family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0638.
    GeneTreeiENSGT00550000074807.
    HOGENOMiHOG000091084.
    KOiK02730.
    OMAiMSRTSYD.
    OrthoDBiEOG7SBP0C.

    Family and domain databases

    Gene3Di3.60.20.10. 1 hit.
    InterProiIPR029055. Ntn_hydrolases_N.
    IPR000426. Proteasome_asu_N.
    IPR023332. Proteasome_suA-type.
    IPR001353. Proteasome_sua/b.
    [Graphical view]
    PfamiPF00227. Proteasome. 1 hit.
    PF10584. Proteasome_A_N. 1 hit.
    [Graphical view]
    SMARTiSM00948. Proteasome_A_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF56235. SSF56235. 1 hit.
    PROSITEiPS00388. PROTEASOME_ALPHA_1. 1 hit.
    PS51475. PROTEASOME_ALPHA_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P21243-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSGAAAASAA GYDRHITIFS PEGRLYQVEY AFKATNQTNI NSLAVRGKDC    50
    TVVISQKKVP DKLLDPTTVS YIFCISRTIG MVVNGPIPDA RNAALRAKAE 100
    AAEFRYKYGY DMPCDVLAKR MANLSQIYTQ RAYMRPLGVI LTFVSVDEEL 150
    GPSIYKTDPA GYYVGYKATA TGPKQQEITT NLENHFKKSK IDHINEESWE 200
    KVVEFAITHM IDALGTEFSK NDLEVGVATK DKFFTLSAEN IEERLVAIAE 250
    QD 252
    Length:252
    Mass (Da):28,001
    Last modified:May 1, 1991 - v1
    Checksum:i5B938C862BC8D7EB
    GO

    Sequence cautioni

    The sequence AAA35020.1 differs from that shown. Reason: Frameshift at position 26.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M31430 Genomic DNA. Translation: AAA35020.1. Frameshift.
    X56971 Genomic DNA. Translation: CAA40292.1.
    M55440 mRNA. Translation: AAA35228.1.
    M63641 Genomic DNA. Translation: AAA34909.1.
    X56732 Genomic DNA. Translation: CAA40056.1.
    S58126 Genomic DNA. Translation: AAD13894.1.
    Z72533 Genomic DNA. Translation: CAA96711.1.
    BK006941 Genomic DNA. Translation: DAA08087.1.
    PIRiS11199. SNBYS1.
    RefSeqiNP_011504.3. NM_001180876.3.

    Genome annotation databases

    EnsemblFungiiYGL011C; YGL011C; YGL011C.
    GeneIDi852873.
    KEGGisce:YGL011C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M31430 Genomic DNA. Translation: AAA35020.1 . Frameshift.
    X56971 Genomic DNA. Translation: CAA40292.1 .
    M55440 mRNA. Translation: AAA35228.1 .
    M63641 Genomic DNA. Translation: AAA34909.1 .
    X56732 Genomic DNA. Translation: CAA40056.1 .
    S58126 Genomic DNA. Translation: AAD13894.1 .
    Z72533 Genomic DNA. Translation: CAA96711.1 .
    BK006941 Genomic DNA. Translation: DAA08087.1 .
    PIRi S11199. SNBYS1.
    RefSeqi NP_011504.3. NM_001180876.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FNT X-ray 3.20 A/O 1-252 [» ]
    1G0U X-ray 2.40 G/U 1-252 [» ]
    1G65 X-ray 2.25 G/U 10-252 [» ]
    1JD2 X-ray 3.00 2/G 10-252 [» ]
    1RYP X-ray 1.90 A/O 10-252 [» ]
    1VSY X-ray 3.00 A/O 10-252 [» ]
    1Z7Q X-ray 3.22 A/O 1-252 [» ]
    2F16 X-ray 2.80 G/U 10-252 [» ]
    2FAK X-ray 2.80 G/U 10-252 [» ]
    2GPL X-ray 2.81 G/U 10-252 [» ]
    2ZCY X-ray 2.90 G/U 1-252 [» ]
    3BDM X-ray 2.70 G/U 1-252 [» ]
    3D29 X-ray 2.60 G/U 12-252 [» ]
    3DY3 X-ray 2.81 G/U 10-252 [» ]
    3DY4 X-ray 2.80 G/U 10-252 [» ]
    3E47 X-ray 3.00 G/U 10-252 [» ]
    3GPJ X-ray 2.70 G/U 10-252 [» ]
    3GPT X-ray 2.41 G/U 10-252 [» ]
    3GPW X-ray 2.50 G/U 10-252 [» ]
    3HYE X-ray 2.50 G/U 10-252 [» ]
    3L5Q X-ray 3.00 A/C 10-252 [» ]
    3MG0 X-ray 2.68 G/U 10-252 [» ]
    3MG4 X-ray 3.11 G/U 10-252 [» ]
    3MG6 X-ray 2.60 G/U 1-252 [» ]
    3MG7 X-ray 2.78 G/U 1-252 [» ]
    3MG8 X-ray 2.59 G/U 1-252 [» ]
    3NZJ X-ray 2.40 G/U 1-252 [» ]
    3NZW X-ray 2.50 G/U 1-252 [» ]
    3NZX X-ray 2.70 G/U 1-252 [» ]
    3OEU X-ray 2.60 G/U 10-252 [» ]
    3OEV X-ray 2.85 G/U 10-252 [» ]
    3OKJ X-ray 2.70 G/U 10-252 [» ]
    3SDI X-ray 2.65 G/U 10-252 [» ]
    3SDK X-ray 2.70 G/U 10-252 [» ]
    3SHJ X-ray 2.80 G/U 10-252 [» ]
    3TDD X-ray 2.70 G/U 10-252 [» ]
    3UN4 X-ray 3.40 G/U 1-252 [» ]
    3UN8 X-ray 2.70 G/U 1-252 [» ]
    4CR2 electron microscopy 7.70 A 1-252 [» ]
    4CR3 electron microscopy 9.30 A 1-252 [» ]
    4CR4 electron microscopy 8.80 A 1-252 [» ]
    4EU2 X-ray 2.51 A/O 10-250 [» ]
    4FZC X-ray 2.80 G/U 10-252 [» ]
    4FZG X-ray 3.00 G/U 10-252 [» ]
    4G4S X-ray 2.49 A 1-252 [» ]
    4GK7 X-ray 2.80 G/U 10-252 [» ]
    4HNP X-ray 2.80 G/U 10-252 [» ]
    4HRC X-ray 2.80 G/U 10-252 [» ]
    4HRD X-ray 2.80 G/U 10-252 [» ]
    4INR X-ray 2.70 G/U 1-252 [» ]
    4INT X-ray 2.90 G/U 1-252 [» ]
    4INU X-ray 3.10 G/U 1-252 [» ]
    4J70 X-ray 2.80 G/U 1-252 [» ]
    4JSQ X-ray 2.80 G/U 1-252 [» ]
    4JSU X-ray 2.90 G/U 1-252 [» ]
    4JT0 X-ray 3.10 G/U 1-252 [» ]
    4LQI X-ray 2.70 G/U 10-252 [» ]
    4NNN X-ray 2.50 G/U 1-252 [» ]
    4NNW X-ray 2.60 G/U 1-252 [» ]
    4NO1 X-ray 2.50 G/U 1-252 [» ]
    4NO6 X-ray 3.00 G/U 1-252 [» ]
    4NO8 X-ray 2.70 G/U 1-252 [» ]
    4NO9 X-ray 2.90 G/U 1-252 [» ]
    4QBY X-ray 3.00 G/U 1-252 [» ]
    ProteinModelPortali P21243.
    SMRi P21243. Positions 10-252.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 33235. 74 interactions.
    DIPi DIP-2810N.
    IntActi P21243. 28 interactions.
    MINTi MINT-525412.

    Protein family/group databases

    MEROPSi T01.971.

    2D gel databases

    UCD-2DPAGE P21243.

    Proteomic databases

    MaxQBi P21243.
    PaxDbi P21243.
    PeptideAtlasi P21243.
    PRIDEi P21243.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YGL011C ; YGL011C ; YGL011C .
    GeneIDi 852873.
    KEGGi sce:YGL011C.

    Organism-specific databases

    CYGDi YGL011c.
    SGDi S000002979. SCL1.

    Phylogenomic databases

    eggNOGi COG0638.
    GeneTreei ENSGT00550000074807.
    HOGENOMi HOG000091084.
    KOi K02730.
    OMAi MSRTSYD.
    OrthoDBi EOG7SBP0C.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-30533-MONOMER.
    Reactomei REACT_100522. Regulation of activated PAK-2p34 by proteasome mediated degradation.
    REACT_189025. ER-Phagosome pathway.
    REACT_189047. Cross-presentation of soluble exogenous antigens (endosomes).
    REACT_189060. Antigen processing: Ubiquitination & Proteasome degradation.
    REACT_189250. AUF1 (hnRNP D0) destabilizes mRNA.
    REACT_83036. Orc1 removal from chromatin.

    Miscellaneous databases

    EvolutionaryTracei P21243.
    NextBioi 972505.
    PROi P21243.

    Gene expression databases

    Genevestigatori P21243.

    Family and domain databases

    Gene3Di 3.60.20.10. 1 hit.
    InterProi IPR029055. Ntn_hydrolases_N.
    IPR000426. Proteasome_asu_N.
    IPR023332. Proteasome_suA-type.
    IPR001353. Proteasome_sua/b.
    [Graphical view ]
    Pfami PF00227. Proteasome. 1 hit.
    PF10584. Proteasome_A_N. 1 hit.
    [Graphical view ]
    SMARTi SM00948. Proteasome_A_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56235. SSF56235. 1 hit.
    PROSITEi PS00388. PROTEASOME_ALPHA_1. 1 hit.
    PS51475. PROTEASOME_ALPHA_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The suppressor gene scl1+ of Saccharomyces cerevisiae is essential for growth."
      Balzi E., Chen W., Capieaux E., McCusker J.H., Haber J.E., Goffeau A.
      Gene 83:271-279(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Proteasomes are essential for yeast proliferation. cDNA cloning and gene disruption of two major subunits."
      Fujiwara T., Tanaka K., Orino E., Yoshimura T., Kumatori A., Tamura T., Chung C.H., Nakai T., Yamaguchi K., Shin S., Kakizuka A., Nakanishi S., Ichihara A.
      J. Biol. Chem. 265:16604-16613(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 174-187 AND 189-198.
    3. "Molecular cloning and functional analysis of three subunits of yeast proteasome."
      Emori Y., Tsukahara T., Kawasaki H., Ishiura S., Sugita H., Suzuki K.
      Mol. Cell. Biol. 11:344-353(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
      Strain: ATCC 26786 / X2180-1A.
    4. "The DNA sequencing of the 17 kb HindIII fragment spanning the LEU1 and ATE1 loci on chromosome VII from Saccharomyces cerevisiae reveals the PDR6 gene, a new member of the genetic network controlling pleiotropic drug resistance."
      Chen W., Balzi E., Capieaux E., Choder M., Goffeau A.
      Yeast 7:287-299(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 46191 / IL125-2B.
    5. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
      Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
      , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
      Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    6. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    7. "Cic1, an adaptor protein specifically linking the 26S proteasome to its substrate, the SCF component Cdc4."
      Jaeger S., Strayle J., Heinemeyer W., Wolf D.H.
      EMBO J. 20:4423-4431(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CIC1.
    8. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    9. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    10. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    12. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
      Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
      Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Structure of 20S proteasome from yeast at 2.4-A resolution."
      Groll M., Ditzel L., Loewe J., Stock D., Bochtler M., Bartunik H.D., Huber R.
      Nature 386:463-471(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 10-252 OF COMPLEX WITH THE 20S PROTEASOME.
    14. "Structural basis for the activation of 20S proteasomes by 11S regulators."
      Whitby F.G., Masters E.I., Kramer L., Knowlton J.R., Yao Y., Wang C.C., Hill C.P.
      Nature 408:115-120(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF COMPLEX WITH THE 20S PROTEASOME.
    15. Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 10-252 OF COMPLEX WITH THE 20S PROTEASOME.
    16. "Crystal structure of the 20 S proteasome:TMC-95A complex: a non-covalent proteasome inhibitor."
      Groll M., Koguchi Y., Huber R., Kohno J.
      J. Mol. Biol. 311:543-548(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 10-252 OF COMPLEX WITH THE 20S PROTEASOME.
    17. "TMC-95-based inhibitor design provides evidence for the catalytic versatility of the proteasome."
      Groll M., Goetz M., Kaiser M., Weyher E., Moroder L.
      Chem. Biol. 13:607-614(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) OF 10-252 OF COMPLEX WITH THE 20S PROTEASOME.
    18. "Crystal structures of salinosporamide A (NPI-0052) and B (NPI-0047) in complex with the 20S proteasome reveal important consequences of beta-lactone ring opening and a mechanism for irreversible binding."
      Groll M., Huber R., Potts B.C.M.
      J. Am. Chem. Soc. 128:5136-5141(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 10-252 OF COMPLEX WITH THE 20S PROTEASOME.
    19. "Crystal structure of the boronic acid-based proteasome inhibitor bortezomib in complex with the yeast 20S proteasome."
      Groll M., Berkers C.R., Ploegh H.L., Ovaa H.
      Structure 14:451-456(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 10-252 OF COMPLEX WITH THE 20S PROTEASOME.
    20. "Structure of a Blm10 complex reveals common mechanisms for proteasome binding and gate opening."
      Sadre-Bazzaz K., Whitby F.G., Robinson H., Formosa T., Hill C.P.
      Mol. Cell 37:728-735(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 10-252 IN COMPLEX WITH THE PROTEASOME.
    21. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (7.4 ANGSTROMS) OF THE 26S PROTEASOME.

    Entry informationi

    Entry nameiPSA1_YEAST
    AccessioniPrimary (citable) accession number: P21243
    Secondary accession number(s): D6VUC6, P15708
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1991
    Last sequence update: May 1, 1991
    Last modified: October 1, 2014
    This is version 168 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 15200 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families
    4. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    5. Yeast chromosome VII
      Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

    External Data

    Dasty 3